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Reviewed, UniProtKB/Swiss-Prot A0JUS3 (DXR_ARTS2)

Last modified November 24, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    1-deoxy-D-xylulose 5-phosphate reductoisomerase
      Short name=DXP reductoisomerase
    EC=1.1.1.267
Alternative name(s):
    1-deoxyxylulose-5-phosphate reductoisomerase
    2-C-methyl-D-erythritol 4-phosphate synthase
Gene names
Name: dxr
Ordered Locus Names: Arth_1399
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity.

Catalytic activity

2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183

Cofactor

Divalent cation By similarity.

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183

Sequence similarities

Belongs to the DXR family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3943941-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183
PRO_1000020215

Regions

Nucleotide binding9 – 3830NADP By similarity

Sites

Metal binding1561Divalent metal cation By similarity
Metal binding1581Divalent metal cation By similarity
Metal binding2271Divalent metal cation By similarity
Binding site1331Substrate By similarity
Binding site1581Substrate By similarity
Binding site1821Substrate By similarity
Binding site2051Substrate By similarity
Binding site2271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JUS3-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 392C63832C6F55DE

FASTA39441,156
        10         20         30         40         50         60 
MQPRRIVLLG STGSIGTQAI DVVDGAPHLF EVVALSAGGG NLELLARQAV HTKAKAVGTA 

        70         80         90        100        110        120 
SGDATALQRL IDDAARATGV AGYRPEIITG PDASTRIAEI EADVVLNGIT GSIGLAPTLA 

       130        140        150        160        170        180 
ALKSGATLAL ANKESLIVGG ALVKAAAREG QIVPVDSEHS AIAQCLRSGT AAEVDRLILT 

       190        200        210        220        230        240 
ASGGPFRGRT REELHNVSPE EALAHPTWDM GLMVTTNSAS LVNKGLEVIE AHLLFDIPLD 

       250        260        270        280        290        300 
RIDVVVHPQS VVHSMVQFVD GSIIAQASPP DMRLPIALGL GWPDRVPKAA TPCDWTQATS 

       310        320        330        340        350        360 
WTFEPLDAEA FPAVNLAKDA AKQGSTYPAV FNAANEEAVM AFHAGRIRFT DIVDTIEAVL 

       370        380        390 
SEHPGSSGLT VESVLDAEAW ARARTHERLA VSSL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000454 Genomic DNA. Translation: ABK02793.1.
RefSeqYP_830893.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0JUS3.

Genome annotation databases

GeneID4446070.
GenomeReviewsGene locus Arth_1399 in contig CP000454_GR.
KEGGart:Arth_1399.
TIGRArth_1399.

Phylogenomic databases

OMAIHSMVEY

Family and domain databases

HAMAPMF_00183.
[Tree]
InterProIPR003821. DXP_reductoisomerase.
IPR013644. DXP_reductoisomerase_C.
IPR013512. DXP_reductoisomerase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF08436. DXP_redisom_C. 1 hit.
PF02670. DXP_reductoisom. 1 hit.
[Graphical view]
PIRSFPIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMsTIGR00243. Dxr. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDXR_ARTS2
AccessionPrimary (citable) accession number: A0JUS3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: November 24, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents